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PMID: 9348285 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Brush border myosin-I structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis.

The Journal of cell biology ·Vol. 139 ·No. 3 ·1997-11-03 ·Pages 683-93

Jontes JD, Milligan RA

Abstract

Brush border myosin-I (BBM-I) is a single-headed myosin found in the microvilli of intestinal epithelial cells, where it forms lateral bridges connecting the core bundle of actin filaments to the plasma membrane. Extending previous observations (Jontes, J.D., E.M. Wilson-Kubalek, and R.A. Milligan. 1995. Nature [Lond.]. 378:751-753), we have used cryoelectron microscopy and helical image analysis to generate three-dimensional (3D) maps of actin filaments decorated with BBM-I in both the presence and absence of 1 mM MgADP. In the improved 3D maps, we are able to see the entire light chain-binding domain, containing density for all three calmodulin light chains. This has enabled us to model a high resolution structure of BBM-I using the crystal structures of the chicken skeletal muscle myosin catalytic domain and essential light chain. Thus, we are able to directly measure the full magnitude of the ADP-dependent tail swing. The approximately 31 degrees swing corresponds to approximately 63 A at the end of the rigid light chain-binding domain. Comparison of the behavior of BBM-I with skeletal and smooth muscle subfragments-1 suggests that there are substantial differences in the structure and energetics of the biochemical transitions in the actomyosin ATPase cycle.

MeSH Terms
Actins/chemistry,ultrastructure Adenosine Diphosphate/chemistry,physiology Animals Calmodulin-Binding Proteins/chemistry,ultrastructure Chickens Crystallography, X-Ray Epithelial Cells/chemistry,ultrastructure Female Freezing Image Processing, Computer-Assisted Intestine, Small/chemistry,ultrastructure Microscopy, Electron/methods Microvilli/chemistry,ultrastructure Models, Molecular Myosin Heavy Chains Myosin Type I Protein Conformation Rabbits
Chemicals
Actins Calmodulin-Binding Proteins MYO1A protein, human Adenosine Diphosphate Myosin Type I Myosin Heavy Chains
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Jontes J D
Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
Milligan R A
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.139.3.683
Published
1997-11-03
Pages
683-93
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2141714
Subset
IM
Grants
NIAMS NIH HHS · AR39155 · United States
NIAMS NIH HHS · AR44278 · United States
External Links
PubMed source DOI: 10.1083/jcb.139.3.683 PMC Full Text View journal details
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